|  |   | 
		| Line 3: | Line 3: | 
|  | <SX load='3j4f' size='340' side='right' viewer='molstar' caption='[[3j4f]], [[Resolution|resolution]] 8.60Å' scene=''> |  | <SX load='3j4f' size='340' side='right' viewer='molstar' caption='[[3j4f]], [[Resolution|resolution]] 8.60Å' scene=''> | 
|  | == Structural highlights == |  | == Structural highlights == | 
| - | <table><tr><td colspan='2'>[[3j4f]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J4F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3j4f]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J4F FirstGlance]. <br> | 
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3j34|3j34]], [[3j3y|3j3y]], [[3j3q|3j3q]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.6Å</td></tr> | 
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1])</td></tr>
 | + |  | 
|  | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j4f OCA], [https://pdbe.org/3j4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j4f RCSB], [https://www.ebi.ac.uk/pdbsum/3j4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j4f ProSAT]</span></td></tr> |  | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j4f OCA], [https://pdbe.org/3j4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j4f RCSB], [https://www.ebi.ac.uk/pdbsum/3j4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j4f ProSAT]</span></td></tr> | 
|  | </table> |  | </table> | 
|  | == Function == |  | == Function == | 
| - | [[https://www.uniprot.org/uniprot/Q79791_9HIV1 Q79791_9HIV1]] Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).[SAAS:SAAS000071_004_008806]  Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).[SAAS:SAAS000071_004_011858]
 | + | [https://www.uniprot.org/uniprot/Q79791_9HIV1 Q79791_9HIV1] Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).[SAAS:SAAS000071_004_008806]  Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).[SAAS:SAAS000071_004_011858] | 
|  | <div style="background-color:#fffaf0;"> |  | <div style="background-color:#fffaf0;"> | 
|  | == Publication Abstract from PubMed == |  | == Publication Abstract from PubMed == | 
| Line 26: | Line 25: | 
|  | __TOC__ |  | __TOC__ | 
|  | </SX> |  | </SX> | 
|  | + | [[Category: Human immunodeficiency virus 1]] | 
|  | [[Category: Large Structures]] |  | [[Category: Large Structures]] | 
| - | [[Category: Meng, X]] | + | [[Category: Meng X]] | 
| - | [[Category: Perilla, J R]] | + | [[Category: Perilla JR]] | 
| - | [[Category: Schulten, K]] | + | [[Category: Schulten K]] | 
| - | [[Category: Zhang, P]] | + | [[Category: Zhang P]] | 
| - | [[Category: Zhao, G]] | + | [[Category: Zhao G]] | 
| - | [[Category: All-atom model]]
 | + |  | 
| - | [[Category: Core]]
 | + |  | 
| - | [[Category: Hexamer]]
 | + |  | 
| - | [[Category: Hiv-1 capsid]]
 | + |  | 
| - | [[Category: Mdff]]
 | + |  | 
| - | [[Category: Tubular assembly]]
 | + |  | 
| - | [[Category: Viral protein]]
 | + |  | 
|  |   Structural highlights   Function Q79791_9HIV1 Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).[SAAS:SAAS000071_004_008806]  Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).[SAAS:SAAS000071_004_011858]
 
  Publication Abstract from PubMed Retroviral capsid proteins are conserved structurally but assemble into different morphologies. The mature human immunodeficiency virus-1 (HIV-1) capsid is best described by a 'fullerene cone' model, in which hexamers of the capsid protein are linked to form a hexagonal surface lattice that is closed by incorporating 12 capsid-protein pentamers. HIV-1 capsid protein contains an amino-terminal domain (NTD) comprising seven alpha-helices and a beta-hairpin, a carboxy-terminal domain (CTD) comprising four alpha-helices, and a flexible linker with a 310-helix connecting the two structural domains. Structures of the capsid-protein assembly units have been determined by X-ray crystallography; however, structural information regarding the assembled capsid and the contacts between the assembly units is incomplete. Here we report the cryo-electron microscopy structure of a tubular HIV-1 capsid-protein assembly at 8 A resolution and the three-dimensional structure of a native HIV-1 core by cryo-electron tomography. The structure of the tubular assembly shows, at the three-fold interface, a three-helix bundle with critical hydrophobic interactions. Mutagenesis studies confirm that hydrophobic residues in the centre of the three-helix bundle are crucial for capsid assembly and stability, and for viral infectivity. The cryo-electron-microscopy structures enable modelling by large-scale molecular dynamics simulation, resulting in all-atom models for the hexamer-of-hexamer and pentamer-of-hexamer elements as well as for the entire capsid. Incorporation of pentamers results in closer trimer contacts and induces acute surface curvature. The complete atomic HIV-1 capsid model provides a platform for further studies of capsid function and for targeted pharmacological intervention.
 Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics.,Zhao G, Perilla JR, Yufenyuy EL, Meng X, Chen B, Ning J, Ahn J, Gronenborn AM, Schulten K, Aiken C, Zhang P Nature. 2013 May 30;497(7451):643-6. doi: 10.1038/nature12162. PMID:23719463[1]
 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
  See Also  References ↑ Zhao G, Perilla JR, Yufenyuy EL, Meng X, Chen B, Ning J, Ahn J, Gronenborn AM, Schulten K, Aiken C, Zhang P. Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular  dynamics. Nature. 2013 May 30;497(7451):643-6. doi: 10.1038/nature12162. PMID:23719463 doi:10.1038/nature12162
 
 |